In situ immobilization of Candida antarctica B lipase in polyurethane foam support

Nyari, Nádia Ligianara Dewes; Fernandes, Ilizandra Aparecida; Bustamante-Vargas, Cindy Elena; Steffens, Clarice; Oliveira, Débora de; Zeni, Jamile; Rigo, Elisandra; Dallago, Rogério Marcos

doi:10.1016/j.molcatb.2015.12.003

Cited by 38 publications

(29 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The immobilized (10.8 g) showed 90.2 U g -1 of hydrolytic activity, corresponding to 974.2 U of total activity, in other words, an immobilization yield of 748.2%. Yields greater than 100%, for this same support, on esterification and hydrolysis activities were reported by Nyari et al (2016) and Bustamante-Vargas et al (2015) for Candida antarctica lipase and (Rohapect ™ DA6L) pectinase enzymes from Aspergillus niger, respectively, both in situ immobilized in polyurethane. These results suggest a beneficial effect of immobilization on the enzyme activity.…”

Section: Efficiency Of Immobilizationsupporting

confidence: 78%

“…In this context, we highlight the enzymatic treatments that correspond to the most recent technology for the biological treatment of effluents (Buss & Henkes, 2014, Silva, Silva, Gois, Almeida, & Abud, 2015 by hydrolytic method reduce the concentration and degrade a large number of toxic and persistent substances (Liu et al, 2011, Baldo et al, 2013, Chen, Zhang, Xu, & Yan, 2013, Zadinelo et al, 2013. The use of immobilized lipase on a suitable support increases the process financial viability, mainly due to its reuse (reaction medium separation), it improves the thermal and mechanical properties (stability at different temperatures), operational stability, storage and the enzymatic activity (Cadena et al 2010, Hu et al, 2012, Palomino-Romero et al, 2012, Colla et al, 2014, Manoel et al, 2015, Nyari, Zeni, Steffens, Dallago, & Rigo, 2015, Shao, Jing, Tian, Zheng, & Shang, 2015, Nyari et al, 2016.…”

Section: Introductionmentioning

confidence: 99%

“…Within this context, the polyurethane (PU) support is highlighted, demonstrating the possibility of lipase in situ during the polymerization stage, presenting excellent activity and yield results in terms of esterification (Nyari et al, 2016). In addition, it has presented chemical compatibility with lipase, resistance to pH, temperature and organic solvents (Simões, Mori, Faria, Castro, & Mendes, 2011, Cui, Tao, Li, Chen, & Tan, 2013, Cipolatti et al, 2015.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Optimization of olive oil hydrolysis process using immobilized Lipase from Burkholderia cepacia sp. in Polyurethane

et al. 2017

Self Cite

View full text Add to dashboard Cite

ABSTRACT. The aim of this study was to achieve the best conditions for the olive oil hydrolysis process at optimal pH and temperature using Burkholderia cepacia lipase immobilized in situ in rigid polyurethane support. The influences of the temperature (13.85 to 56.5ºC) and pH (4.18 to 9.82) were evaluated by a central composite rotational experimental design 2 2 . The operational stability and storage conditions were also studied. The olive oil hydrolysis process was optimized in pH 7.0, at 40°C and 15 min of reaction, with 66 and 93 U g -1 of hydrolysis activity in free and immobilized lipase, respectively, with > 700% yield. The immobilized remained stable for up to 40 days of storage at temperatures of 60 o C, and for 100 days from 4 to 25°C. The operational stability of the immobilized was 6 continuous cycles. In this way, immobilization showed to be a promising alternative for its application in olive oil hydrolysis, having storage stability and reuse capability. Otimização do processo de hidrólise do azeite de oliva utilizando lipase Burkholderia cepacia sp. imobilizada em poliuretano RESUMO. As lipases são enzimas que, naturalmente, atuam na hidrólise de óleos e gorduras, porém, em meios com quantidade baixa de água, são capazes de atuar em reações como a esterificação, alcoólise, acidólise, aminólise, entre outras. Sendo utilizadas na redução da concentração dos lipídios contidos nos efluentes, promovendo a hidrólise dos óleos e gorduras presentes. Sendo assim, o objetivo do presente estudo foi obter as melhores condições do processo de hidrólise do óleo de oliva em termos de pH e temperatura, utilizando lipase de Burkholderia cepacia imobilizada in situ em suporte rígido de poliuretano. O processo de hidrólise do óleo de oliva foi obtido utilizando as condições de pH de 7,0, temperatura de 40°C e 15 min de reação com atividade hidrolítica para a enzima livre e imobilizada de 66 e 93 U g -1 respectivamente, com rendimento de > 700%. O imobilizado apresentou estabilidade de 40 dias de estocagem nas temperaturas de 60ºC e 100 dias de armazenamento nas temperaturas entre -4 a 25ºC e a estabilidade operacional de 6 ciclos contínuos. O imobilizado se mostrou uma alternativa promissora para aplicação no processo de hidrólise frente à enzima livre, tendo estabilidade de estocagem e possibilidade de reutilização operacional.Palavras-chaves: biocatálise, lipase, imobilização in situ, poliuretano, hidrólise.

show abstract

Section: Efficiency Of Immobilizationsupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Optimization of olive oil hydrolysis process using immobilized Lipase from Burkholderia cepacia sp. in Polyurethane

et al. 2017

Self Cite

View full text Add to dashboard Cite

show abstract

“…The immobilized yield was calculated considering the total activity of the free lipase in solution given on the immobilization process (that considers the volume of the enzymatic extract employed on the immobilization test and its activity (U/mL)) and the immobilized total activity (that considers the total mass of the produced immobilized and its activity (U/g)) according to Equation 2 (Nyari et al, 2016).…”

Section: Immobilization Yieldmentioning

confidence: 99%

“…Later, the dosage of enzyme esterification activity was measured using oleic acids as substrate. After each cycle, the immobilized was washed with 50 mL of ethanol and the moisture equalized in a vacuum pump during 30 min (Nyari et al, 2016).…”

Section: Stability Of Free and Immobilized Enzyme At High And Low Temmentioning

confidence: 99%

In situ immobilization of commercial lipase in rigid polyurethane foam and application in the esterification of geraniol and oleic acid

et al. 2017

Self Cite

View full text Add to dashboard Cite

The aim of this work was to evaluate the immobilization of Candida antarctica lipase B (CalB) using polyurethane (PU) foam. The stability of the enzymatic derivative against temperature (40, 60 and 80 °C) together with the recycle capacity and storage stability (4 and 25°C) were evaluated. The application of the enzymatic derivative of CalB in esterification reactions was accomplished. Results indicated that the molar ratio between polyol and isocyanate monomers of 5:3 (v/v) was the best one for the immobilization. The immobilization process resulted in a 1363% increase in activity for the enzymatic derivative. The enzymatic derivative obtained kept its initial activity even after 21 h of exposure to high temperatures. The enzymatic activity of the complex was maintained during 30 days at low temperatures, and showed stability during 4 consecutive reuse cycles. The synthesis of geranyl oleate catalyzed by the immobilized derivative presented conversion of 87%. Taking into account the promising results obtained, the low cost of the immobilization support employed and the whole technique developed, this work comprise an innovative contribution.

show abstract

Application of Stemphylium lycopersici Extracts Immobilized on MCM‐48type Mesoporous Materials as Biocatalysts for Monoacylglycerol Production

Paranhos,

Dallago,

dos S. Martins

et al. 2024

Chemistry & Biodiversity

Self Cite

View full text Add to dashboard Cite

Monoacylglycerols are eco‐friendly and inexpensive emulsifiers with a range of applications. The traditional synthetic route is not eco‐friendly, while enzymatic catalysis offers milder reaction conditions and higher selectivity. However, its application still is limited due to the costs. In this context, endophytic fungi can be source to new biocatalysts with enhanced catalytic activity. Based on this perspective, the aim of this study was perform the synthesis of MAG‘s through transesterification reactions of solketal and different vinyl esters, using crude and immobilized lipolytic extracts from the endophytic fungi Stemphylium lycopersici, isolated from Humiria balsamifera. The reactions were conducted using 100 mg of biocatalyst, 1 mmol of substrates, 9 : 1 n‐heptane/acetone, at 40 °C, 200 rpm for 96 h. In the reactions using the ILE and stearate, laureate and decanoate vinyl esters it was possible to obtain the correspondent products with conversion rates of 52–75 %. Also, according to the structure drivers used in MCM‐48 synthesis, different morphologies and conversions rates were observed. Employing [C16MI] Cl, [C14MI] Cl and [C4MI] Cl, the 1‐lauroyl‐ glycerol conversion was 36 %, 79 % and 44 %, respectively. This is the first work involving the immobilization of an endophytic fungi and its utilization as a biocatalyst in the production of MAG's.

show abstract

In situ immobilization of Candida antarctica B lipase in polyurethane foam support

Cited by 38 publications

References 35 publications

<b>Optimization of olive oil hydrolysis process using immobilized Lipase from <i>Burkholderia cepacia</i> sp. in Polyurethane

<b>Optimization of olive oil hydrolysis process using immobilized Lipase from <i>Burkholderia cepacia</i> sp. in Polyurethane

In situ immobilization of commercial lipase in rigid polyurethane foam and application in the esterification of geraniol and oleic acid

Application of Stemphylium lycopersici Extracts Immobilized on MCM‐48type Mesoporous Materials as Biocatalysts for Monoacylglycerol Production

Contact Info

Product

Resources

About